Table of Contents Author Guidelines Submit a Manuscript
Journal of Chemistry
Volume 2013 (2013), Article ID 453056, 4 pages
Research Article

Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine 𝛽 -Lactoglobulin

1Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
2Department of Biological Sciences, Tarbiat Moallem University, Tehran, Iran
3Chemistry Department, Faculty of Science, Islamic Azad University, Takestan Branch, Takestan, Iran
4Chemistry Department, Imam Khomeini International University, Qazvin, Iran

Received 5 June 2012; Revised 30 July 2012; Accepted 13 August 2012

Academic Editor: Yehia Mechref

Copyright © 2013 Adeleh Divsalar et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


We have investigated the interactions between β-lactoglobulin, BLG, and new synthesized Cu(II) complex (2,2′-dibipyridine Cu(II) chloride) using isothermal titration calorimetry (ITC) methods at different temperatures of 298 and 310 K. The heats of BLG + Cu(II) interactions are reported and analyzed in terms of the extended solvation theory for calculation of binding and thermodynamic parameters of the interaction. The results suggested that binding of Cu(II) complex on BLG resulted in significant changes on the tertiary structure and conformation of protein via increasing of hydrophobicity and inducing partially unfolded structure in BLG which has a good agreement with the solvation parameters recovered by the extended solvation model suggesting destabilization of the protein.